ID A0A197K4M6_9FUNG Unreviewed; 765 AA.
AC A0A197K4M6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN ORFNames=K457DRAFT_72151 {ECO:0000313|EMBL:OAQ31419.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ31419.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ31419.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ31419.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV442030; OAQ31419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197K4M6; -.
DR STRING; 1314771.A0A197K4M6; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:OAQ31419.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 39..467
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 663..690
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 765 AA; 85255 MW; E1A58E1FCD44642C CRC64;
MAANTTNVSR QQPPWRVPEG KPVPKLKLYN SMTRTKTEFV PMDGNQVTWY ACGPTVYDST
HIGHARNYVS LDILHRVIED YFGYNVLFVE NITDIDDKII KRARQNHLFN NFKAATTTVT
PEAIAKAEAA WKLYADSELK AIDATAADQW VAFVEKINKD AALKSSLTTA HPKFPMHFSA
LQEAYDAIEQ AKKDAGKADA TAFCDANKTT LSNLLDKELS HTVSDPKVFR DLAAYWEGEF
FKDMDRLGVR RPDVLTRVSE YVPEIVDFVK KIISNGYAYE AEGSVYFDTA AFDGKDGHHY
AKLAPWSKGD AALMEESEGS LGIKLSGKKS SMDFALWKAS KSGEPAWDSP WGPGRPGWHI
ECSVMASEVL GSGMDIHSGG IDLAFPHHDN ELAQSEAYHQ CDQWVNYFTH CGHLHVEGQK
MSKSLKNFIS VQQALEKYTP RQLRFFFLLH QWDTGVDFRD TSMSEAMSVE TTFNNFFANA
KAMIAEAKHT ALDSTGTHNF RRLELDMIVA LKDKQNAVHA ALCDSINTPN AMSELQALVS
RTNVYIKEAG SNLNVEVVNK VALYVSKILR TFGLDGVVSD PIGFASAEAG GASVEDVAMP
YLQVLSTFRD TIRAYAREGR PVQEMLALSD KLRDEDLERL GVSLDDREDG KALIKFIPAE
ELAAQRQAKI QQAAEKAARK EEAAKAKEAA RLLKLEKGKV SQLEMFKVAA NSAEYGSFDE
SGIPVTDKEG QELPKSRRKK LQKEWDVQKK LHEDYLAEKA KGTIA
//
